AMPP2_PHANO
ID AMPP2_PHANO Reviewed; 789 AA.
AC Q0V147;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable Xaa-Pro aminopeptidase SNOG_02267;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN ORFNames=SNOG_02267;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; CH445327; EAT90479.2; -; Genomic_DNA.
DR RefSeq; XP_001792881.1; XM_001792829.1.
DR AlphaFoldDB; Q0V147; -.
DR SMR; Q0V147; -.
DR STRING; 13684.SNOT_02267; -.
DR EnsemblFungi; SNOT_02267; SNOT_02267; SNOG_02267.
DR GeneID; 5969731; -.
DR KEGG; pno:SNOG_02267; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; Q0V147; -.
DR OrthoDB; 352329at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..789
FT /note="Probable Xaa-Pro aminopeptidase SNOG_02267"
FT /id="PRO_0000411847"
FT REGION 607..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 789 AA; 88042 MW; 4D7A2DD2C9977BAF CRC64;
MEVLDATSLA ERLKWEAKGY WLHFEAETPL EKYPAKQHAR RVQEKLGIEE GLIYLSGQQA
RNNEDSDMPA PFRQLRYFYY LSGGPTLAEA LVKYDVDEVY YSDEVSDYII DWYHHSCNRG
KLYTLHDPAK SPIGNHHAPI DSVSLQPAMN VARMIKDEHE IKLIRKANDI SSKAHREVLS
NILKFTNEAQ VEGLFLDVCV SHQAKQQAYD PIAASGPNAG TLHYDANDED FGKRQLMCLD
AGCEYELYAS DITRTFPLSS KWPSKEAANI YRLVERMQEL CIKRLAPGVR YLDLHILAHQ
IAIDGLLALG ILHNGTKEEI YKAGTSRAFF PHGLGHHIGL EVHDVGQAEL MSVRRGKQVL
EQSSHLEEGM IVTVEPGIYF SVYALQHFYL PSPVHSKYIN LEVLNRYLPV GGVRIEDDIL
ITAKSYENLT TAPKGDEMLE IIQRGRSNVN SIPARRQSGR TQITEDEPPL LRAPGISAST
PQSILRPIAR SSTMPAELKQ DKSVDFEPFE GPSLFSNFRR SMTTDEKIQR WQQDHIPTTA
TRINLTPSSQ YKSVCGSNTR EVKHVYMISG SFPPGTARGA LREQILPACK QCTILCETLD
RLRQSLSMSK ESPEAELDVS PVISQKQIRN RRSVSSTARH DLRGDRERPQ HSPMTGLANG
LSAMCLEPLN HVSESPTPSQ RRAGGCTPHW RGQNRADQSG DDALRAAQET QILQSKPSVR
SNPATDQLSA KAVSDVLLEL QRQGPAAGSD RCTLGKQEGV EGIPAISRAK NFHVSTGGSM
VGEARRAEE
